View source for 1jyo


==Structure of the Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP==
<StructureSection load='1jyo' size='340' side='right'caption='[[1jyo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jyo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JYO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyo OCA], [https://pdbe.org/1jyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jyo RCSB], [https://www.ebi.ac.uk/pdbsum/1jyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jyo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SICP_SALTY SICP_SALTY] Molecular chaperone required for sptP stabilization and secretion.
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== Publication Abstract from PubMed ==
Many bacterial pathogens use a type III protein secretion system to deliver virulence effector proteins directly into the host cell cytosol, where they modulate cellular processes. A requirement for the effective translocation of several such effector proteins is the binding of specific cytosolic chaperones, which typically interact with discrete domains in the virulence factors. We report here the crystal structure at 1.9 A resolution of the chaperone-binding domain of the Salmonella effector protein SptP with its cognate chaperone SicP. The structure reveals that this domain is maintained in an extended, unfolded conformation that is wound around three successive chaperone molecules. Short segments from two different SptP molecules are juxtaposed by the chaperones, where they dimerize across a hydrophobic interface. These results imply that the chaperones associated with the type III secretion system maintain their substrates in a secretion-competent state that is capable of engaging the secretion machinery to travel through the type III apparatus in an unfolded or partially folded manner.

Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion.,Stebbins CE, Galan JE Nature. 2001 Nov 1;414(6859):77-81. PMID:11689946<ref>PMID:11689946</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1jyo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Galan JE]]
[[Category: Stebbins CE]]